Journal of Dairy Science
Volume 93, Issue 9 , Pages 3910-3924 , September 2010

A methodology for monitoring globular milk protein changes induced by ultrafiltration: A dual structural and functional approach

  • M. Van Audenhaege

      Affiliations

    • INRA, UMR1253 Science et Technologie du Lait et de l’Œuf, 35042 Rennes, France
    • Agrocampus Ouest, UMR1253 Science et Technologie du Lait et de l’Œuf, 35042 Rennes, France
    • Corresponding Author InformationCorresponding authors.
  • ,
  • J. Belmejdoub

      Affiliations

    • Université Rennes 1, UMR6226 Sciences Chimiques de Rennes, CNRS, 35042 Rennes, France
    • Université européenne de Bretagne, 35000 Rennes, France
  • ,
  • D. Dupont

      Affiliations

    • INRA, UMR1253 Science et Technologie du Lait et de l’Œuf, 35042 Rennes, France
    • Agrocampus Ouest, UMR1253 Science et Technologie du Lait et de l’Œuf, 35042 Rennes, France
  • ,
  • A. Chalvin

      Affiliations

    • INRA, UMR1253 Science et Technologie du Lait et de l’Œuf, 35042 Rennes, France
    • Agrocampus Ouest, UMR1253 Science et Technologie du Lait et de l’Œuf, 35042 Rennes, France
  • ,
  • S. Pezennec

      Affiliations

    • INRA, UMR1253 Science et Technologie du Lait et de l’Œuf, 35042 Rennes, France
    • Agrocampus Ouest, UMR1253 Science et Technologie du Lait et de l’Œuf, 35042 Rennes, France
  • ,
  • Y. Le Gouar

      Affiliations

    • INRA, UMR1253 Science et Technologie du Lait et de l’Œuf, 35042 Rennes, France
    • Agrocampus Ouest, UMR1253 Science et Technologie du Lait et de l’Œuf, 35042 Rennes, France
  • ,
  • F. Garnier-Lambrouin

      Affiliations

    • INRA, UMR1253 Science et Technologie du Lait et de l’Œuf, 35042 Rennes, France
    • Agrocampus Ouest, UMR1253 Science et Technologie du Lait et de l’Œuf, 35042 Rennes, France
  • ,
  • M. Rabiller-Baudry

      Affiliations

    • Université Rennes 1, UMR6226 Sciences Chimiques de Rennes, CNRS, 35042 Rennes, France
    • Université européenne de Bretagne, 35000 Rennes, France
  • ,
  • G. Gesan-Guiziou

      Affiliations

    • INRA, UMR1253 Science et Technologie du Lait et de l’Œuf, 35042 Rennes, France
    • Agrocampus Ouest, UMR1253 Science et Technologie du Lait et de l’Œuf, 35042 Rennes, France
    • Corresponding Author InformationCorresponding authors.

Received 14 December 2009 ,Accepted 22 May 2010.

References 

  1. Bowen WR, Gan Q. Properties of microfiltration membranes: The effects of adsorption and shear on the recovery of an enzyme. Biotechnol. Bioeng. 1992;40:491–497
  2. Campbell MJ, Walter RP, McLoughlin R, Knowles CJ. Effect of temperature on protein conformation and activity during ultrafiltration. J. Membr. Sci. 1993;78:35–43
  3. Charm SE, Lai CJ. Comparison of ultrafiltration systems for concentration of biologicals. Biotechnol. Bioeng. 1971;13:185–202
  4. Chrysina ED, Brew K, Acharya KF. Crystal structures of apo- and holo-bovine α-lactalbumin at 2.2-Å resolution reveal an effect of calcium on inter-lobe interactions. J. Biol. Chem. 2000;275:37021–37029
  5. Denis S, Terré S, Bertheau Y, Boyaval P. Factors affecting pectate lyase activity during membrane filtration. Biotechnol. Tech. 1990;4:127–132
  6. Dumon S, Barnier H. Ultrafiltration of protein solutions on ZrO2 membranes. The influence of surface chemistry and solution chemistry on adsorption. J. Membr. Sci. 1992;74:289–302
  7. Dupont D, Rolet-Répécaud O, Muller-Renaud S. Determination of the heat treatment undergone by milk by following the denaturation of α-lactalbumin with a biosensor. J. Agric. Food Chem. 2004;52:677–681
  8. Elgar DF, Carmen SN, Ayers JS, Pritchard M, Otter DE, Palmano KP. Simultaneous separation and quantitation of the major bovine whey proteins including proteose peptone and caseinomacropeptide by reversed-phase high-performance liquid chromatography on polystyrene-divinylbenzene. J. Chromatogr. A. 2000;878:183–196
  9. Geng X, Regnier FE. Retention model for proteins in reversed-phase liquid chromatography. J. Chromatogr. 1984;296:15–30
  10. Harris JL, Pecar MA, Pearce RJ. Effect of the processing equipment on protein functionality in the concentration of cheese whey by ultrafiltration. Aust. J. Dairy Technol. 1989;44:78–81
  11. Herceg Z, Lelas V, Režek A. Functional properties of α-lactalbumin and β-lactoglobulin. Mljekarstvo. 2004;54:195–208
  12. International Dairy Federation. Milk—Determination of nitrogen content—Part 1: Kjeldahl method. Brussels, Belgium: International Dairy Federation; 2001;FIL-IDF standard 20-1, ISO 8968-1
  13. International Dairy Federation. Dried milk protein products—Determination of nitrogen solubility index. Brussels, Belgium: International Dairy Federation; 2002;FIL-IDF standard 173, ISO 15323
  14. Jeanson S, Dupont D, Grattard N, Rolet-Répécaud O. Characterization of the heat treatment undergone by milk using two inhibition ELISAs for quantification of native and heat denatured α-lactalbumin. J. Agric. Food Chem. 1999;47:2249–2254
  15. Jolliffe IT. Principal Component Analysis. New York, NY: Springer Verlag; 1986;
  16. Kato A, Nakai S. Hydrophobicity determined by a fluorescent probe method and its correlation with surface properties of proteins. Biochim. Biophys. Acta. 1980;624:13–20
  17. Kella NKD, Yang ST, Kinsella JE. Effect of disulfide bond cleavage on structural and interfacial properties of whey proteins. J. Agric. Food Chem. 1989;37:1203–1210
  18. Kronman MJ, Andreotti R, Vitols R. Inter- and intra-molecular interactions of α-lactalbumin. I. The apparent heterogeneity at acid pH. Biochem. 1964;3:1145–1160
  19. Lefèvre T, Subirade M. Structural and interaction properties of β-lactoglobulin as studied by FTIR spectroscopy. Int. J. Food Sci. Technol. 1999;34:419–428
  20. Lemoine R. Le lait source de nouvelles promesses. Revue Laitière Française. 2005;657:32–33
  21. Mangino ME, Huffman LM, Regester GO. Changes in the hydrophobicity and functionality of whey during the processing of whey protein concentrates. J. Food Sci. 1988;53:1684–1686
  22. Maruyama T, Katoh S, Nakajima M, Nabetani H. Mechanism of bovine serum albumin aggregation during ultrafiltration. Biotechnol. Bioeng. 2001;75:233–238
  23. McKenzie HA, Murphy WH. General Methods and Elemental Analysis. New York, NY: Milk Proteins, Chemistry and Molecular Biology. Academic Press; 1971;
  24. Mehra RK, Donnelly W. Fractionation of whey protein components through a large pore size hydrophilic cellulose membrane. J. Dairy Res. 1993;60:89–97
  25. Meireles M, Aimar P, Sanchez V. Albumin denaturation during ultrafiltration: Effects of operating conditions and consequences on membrane fouling. Biotechnol. Bioeng. 1991;38:528–534
  26. Muller A, Chaufer B, Merin U, Daufin G. Prepurification of α-lactalbumin with ultrafiltration ceramic membranes from acid casein whey: Study of operating conditions. Lait. 2003;83:111–129
  27. Narendranathan TJ, Dunnill P. The effect of shear on globular proteins during ultrafiltration: Studies of alcohol dehydrogenase. Biotechnol. Bioeng. 1982;24:2103–2107
  28. Permyakov EA, Yarmolenko VV, Kalinichenko LP, Morozova LA, Burstein EA. Calcium binding to alpha-lactalbumin: Structural rearrangement and association constant evaluation by means of intrinsic protein fluorescence changes. Biochem. Biophys. Res. Commun. 1981;100:191–197
  29. Portugal CAM, Crespo JG, Lima JC. Monitoring the structural alterations induced in β-lactoglobulin during ultrafiltration: Learning from chemical and thermal denaturation phenomena. J. Membr. Sci. 2007;300:211–223
  30. Portugal CAM, Lima JC, Crespo JG. Probing the change of enzymatic activity of horseradish peroxidase induced by membrane permeation using tryptophan fluorescence. J. Membr. Sci. 2006;284:180–192
  31. Portugal CAM, Lima JC, Crespo JG. Effect of physicochemical conditions on the ultrafiltration of β-lactoglobulin: Fluorescence probing of induced structural changes. J. Membr. Sci. 2008;321:69–80
  32. Putnam FW. The Plasma Proteins: Structure, Function and Genetic Control. ed. Academic Press, New York, NY: Vol. 1. F. W. Putnam; 1975;
  33. R Development Core Team. 2008. R: A language and environment for statistical computing. R Foundation for Statistical Computing, Vienna, Austria.
  34. Resmini P, Pellegrino L, Andreini R, Prati F. Determinazione delle sieroproteine solubili del latte per HPLC (cromatographia liquida ad alta prestazione) in fase inversa. Sci. Tecn. Latt. Cas. 1989;40:7–23
  35. Roger, L., J. L. Maubois, G. Brulé, and M. Piot. 1981. Process for obtaining an alpha-lactalbumin enriched product from whey, and uses thereof. US Pat. No. 4,485,040.
  36. Themistou E, Singh I, Shang C, Balu-Iyer SV, Alexandridis P, Neelamegham S. Application of fluorescence spectroscopy to quantify shear-induced protein conformation change. Biophys. J. 2009;97:2567–2576
  37. Towsend AA, Nakai S. Relationship between protein hydrophobicity and foaming characteristics of food proteins. J. Food Sci. 1983;48:588–594
  38. Truskey GA, Gabler R, DiLeo A, Manter T. The effect of membrane filtration upon protein conformation. J. Parenter. Sci. Technol. 1987;41:180–193
  39. Vedantham G, Carothers SL, Belfort G, Przybycien TM. Structural response of bovine growth hormone to dead-end ultrafiltration. Sep. Sci. Technol. 2003;38:251–270
  40. Zydney AL. Protein separations using membrane filtration: New opportunities for whey fractionation. Int. Dairy J. 1998;8:243–250

PII: S0022-0302(10)00415-7

doi: 10.3168/jds.2009-2995

Journal of Dairy Science
Volume 93, Issue 9 , Pages 3910-3924 , September 2010